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  Actin crosslinker competition and sorting drive emergent GUV size-dependent actin network architecture

Bashirzadeh, Y., Redford, S. A., Lorpaiboon, C., Groaz, A., Litschel, T., Schwille, P., et al. (2020). Actin crosslinker competition and sorting drive emergent GUV size-dependent actin network architecture. bioRxiv, 10.03.322354. doi:10.1101/2020.10.03.322354.

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 Creators:
Bashirzadeh, Yashar, Author
Redford, Steven A., Author
Lorpaiboon, Chatipat, Author
Groaz, Alessandro, Author
Litschel, Thomas1, Author              
Schwille, Petra1, Author              
Hocky, Glen M., Author
Dinner, Aaron R., Author
Liu, Allen P., Author
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1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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 Abstract: The proteins that make up the actin cytoskeleton can self-assemble into a variety of structures. In vitro experiments and coarse-grained simulations have shown that the actin crosslinking proteins α-actinin and fascin segregate into distinct domains in single actin bundles with a molecular size-dependent competition-based mechanism. Here, by encapsulating actin, α-actinin, and fascin in giant unilamellar vesicles (GUVs), we show that physical confinement can cause these proteins to form much more complex structures, including rings and asters at GUV peripheries and centers; the prevalence of different structures depends on GUV size. Strikingly, we found that α-actinin and fascin self-sort into separate domains in the aster structures with actin bundles whose apparent stiffness depends on the ratio of the relative concentrations of α-actinin and fascin. The observed boundary-imposed effect on protein sorting may be a general mechanism for creating emergent structures in biopolymer networks with multiple crosslinkers.

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 Dates: 2021-02-112020-10-03
 Publication Status: Published online
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 Rev. Type: No review
 Identifiers: DOI: 10.1101/2020.10.03.322354
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Title: bioRxiv
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Pages: - Volume / Issue: - Sequence Number: 10.03.322354 Start / End Page: - Identifier: -